ID A0A091GIW3_9AVES Unreviewed; 884 AA.
AC A0A091GIW3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
DE Flags: Fragment;
GN ORFNames=N303_05998 {ECO:0000313|EMBL:KFO81266.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO81266.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO81266.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO81266.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for glutamate that functions as a ligand-gated ion
CC channel in the central nervous system and plays an important role in
CC excitatory synaptic transmission. L-glutamate acts as an excitatory
CC neurotransmitter at many synapses in the central nervous system.
CC {ECO:0000256|RuleBase:RU367118}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367118};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}.
CC Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000256|RuleBase:RU367118}.
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DR EMBL; KL448199; KFO81266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GIW3; -.
DR STRING; 55661.A0A091GIW3; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR CDD; cd06382; PBP1_iGluR_Kainate; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_Glu_rcpt_met.
DR InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR InterPro; IPR001320; Iontro_rcpt_C.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR18966:SF174; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 3; 1.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367118};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU367118};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU367118};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286,
KW ECO:0000256|RuleBase:RU367118};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257,
KW ECO:0000256|RuleBase:RU367118};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|RuleBase:RU367118};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367118};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367118};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367118}.
FT TRANSMEM 530..549
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 606..628
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 786..810
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 400..767
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 410..474
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO81266.1"
FT NON_TER 884
FT /evidence="ECO:0000313|EMBL:KFO81266.1"
SQ SEQUENCE 884 AA; 99900 MW; CF297C02C2960D25 CRC64;
CLAGGIFEYA DGPNTQVMSA EEQAFRFSAN IINRNRTLLP NTTLTYDIQR IHFHDSFEAT
KKACDQLALG VVAIFGPSQG SCTNAVQSIC NALEVPHIQL RWKHHPLDNK DSFYVNLYPD
YASLSHAILD LVQYLKWRSA TVVYDDSTGL IRLQELIMAP SRYNIRLKIR QLPLDTDDAR
PLLKEMKRGR EFRIIFDCSH LMAAQILKQA MAMGMMTEYY HFIFTTLDLY ALDLEPYRYS
GVNLTGFRIL NVENPHVSSI IEKWSMERLQ SAPKAELGLL DGVMMTDAAL LYDAVHVVSV
CYQRAPQMTV NSLQCHRHKA WRFGGRFMNF IKEAQWEGLT GRIVFNKTSG LRTDFDLDIV
SLKEDGLEKV GAWSPSDGLN ITEISKGRGP NVTDSLSNRS LIVTTVLEEP FVMFRKSDTA
LFGNDRFEGY CIDLLKELAI ILGFTYEIRL VEDGKYGAQD EKGQWNGMIK ELIDHKADLA
VAPLTITHVR EKAIDFSKPF MTLGVSILYR KPNGTNPSVF SFLNPLSPDI WMYILLAYLG
VSCVLFVIAR FSPYEWYDAH PCNPGSDIVE NNFTLFNSFW FGMGALMQQG SELMPKALST
RIIGGIWWFF TLIIISSYTA NLAAFLTVER MESPIDSADD LAKQTKIEYG AVKDGATMTF
FKKSKISTFE KMWAFMSSKP TALVKNNEEG IQRTLTADYA LLMESTTIEY ITQRNCNLTQ
IGGLIDSKGY GIGTPMGSPY RDKITIAILQ LQEEDKLHVM KEKWWRGNGC PEDENKEASA
LGIQNIGGIF IVLAAGLVLS VFVAMVEFIY KLRKTAEREQ RSFCSAMADE IRLSLTCQRR
VKHKPQPPVM VKTDAVINMH TFNDRRLPGK DNMTCNTGLT PVFP
//
